ID S5XVP4_PARAH Unreviewed; 432 AA.
AC S5XVP4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=JCM7686_2282 {ECO:0000313|EMBL:AGT09352.1};
OS Paracoccus aminophilus JCM 7686.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT09352.1, ECO:0000313|Proteomes:UP000015480};
RN [1] {ECO:0000313|EMBL:AGT09352.1, ECO:0000313|Proteomes:UP000015480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT09352.1};
RX PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA Schluter A., Puhler A., Bartosik D.;
RT "Architecture and functions of a multipartite genome of the methylotrophic
RT bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT chromids.";
RL BMC Genomics 15:124-124(2014).
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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DR EMBL; CP006650; AGT09352.1; -; Genomic_DNA.
DR RefSeq; WP_020950990.1; NC_022041.1.
DR AlphaFoldDB; S5XVP4; -.
DR STRING; 1367847.JCM7686_2282; -.
DR KEGG; pami:JCM7686_2282; -.
DR PATRIC; fig|1367847.3.peg.2274; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR HOGENOM; CLU_042042_4_2_5; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000015480; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd02940; DHPD_FMN; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005720; Dihydroorotate_DH_cat.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01180; DHO_dh; 1.
DR Pfam; PF14697; Fer4_21; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AGT09352.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015480}.
FT DOMAIN 337..369
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 370..400
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 411..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 432 AA; 47199 MW; FB339795EB5E58EB CRC64;
MADLRSNFIG IKSPNPFWLA SAPPTDKEVN VRRAFQAGWG GVVWKTLGLE GPPVVNVNGP
RYGVVYGADR RVLGINNIEL ITDRPLEVNL REIKSVKRDY PDRALIISLM VPCDEPSWIS
ILRAIEDTEA DGVELNFGCP HGMAERGMGA AVGQVPEYIE MVTRWVKQHS RMPCIVKLTP
NITDVKKPAE AALRGGADAV SLINTVNSIT SVDLDLFAPQ PTIDGKGSHG GYCGPAVKPI
ALNMVAEIAR NPATANLPIS GIGGVTTWRD AAEFMALGAG NVQVCTAAMT YGFKVVQEMI
TGLHDYLDSH EMEMSDLIRR AVPNVTDWQH LNLNYTTKAV INQDDCIKCG RCYAACEDTS
HQAINIEPGR VFKVNEAECV ACNLCVDVCP VENCITMREL EVGEMDLRTG RPVQPYSNWT
EHPNNPMARA AE
//
